SitesBLAST
Comparing HSERO_RS21870 FitnessBrowser__HerbieS:HSERO_RS21870 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 89% coverage: 8:459/506 of query aligns to 6:475/490 of 4yjiA
- active site: K79 (= K81), S158 (= S156), S159 (= S157), G179 (≠ T177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L83), G132 (= G130), S158 (= S156), G179 (≠ T177), G180 (= G178), A182 (≠ S180)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 86% coverage: 8:443/506 of query aligns to 6:460/485 of 2f2aA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding glutamine: G130 (= G132), S154 (= S156), D174 (= D176), T175 (= T177), G176 (= G178), S178 (= S180), F206 (≠ G208), Y309 (≠ D300), Y310 (≠ V301), R358 (≠ N340), D425 (≠ W407)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 86% coverage: 8:443/506 of query aligns to 6:460/485 of 2dqnA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding asparagine: M129 (≠ A131), G130 (= G132), T175 (= T177), G176 (= G178), S178 (= S180), Y309 (≠ D300), Y310 (≠ V301), R358 (≠ N340), D425 (≠ W407)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 91% coverage: 5:466/506 of query aligns to 2:475/478 of 3h0mA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding glutamine: M122 (≠ A131), G123 (= G132), D167 (= D176), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (≠ G208), Y302 (≠ D300), R351 (≠ N340), D418 (≠ E395)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 91% coverage: 5:466/506 of query aligns to 2:475/478 of 3h0lA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding asparagine: G123 (= G132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (≠ D300), R351 (≠ N340), D418 (≠ E395)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 87% coverage: 19:458/506 of query aligns to 140:589/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 177:180) binding
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ L235) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 87% coverage: 19:458/506 of query aligns to 140:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G130), T258 (≠ A133), S281 (= S156), G302 (≠ T177), G303 (= G178), S305 (= S180), S472 (≠ N340), I532 (≠ G398), M539 (≠ Y405)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 89% coverage: 10:461/506 of query aligns to 2:458/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 89% coverage: 9:458/506 of query aligns to 6:445/457 of 5h6sC
- active site: K77 (= K81), S152 (= S156), S153 (= S157), L173 (≠ T177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G130), R128 (≠ G132), W129 (≠ A133), S152 (= S156), L173 (≠ T177), G174 (= G178), S176 (= S180), W306 (≠ I313), F338 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 85% coverage: 11:439/506 of query aligns to 4:430/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 90% coverage: 3:457/506 of query aligns to 23:487/507 of Q84DC4
- T31 (≠ V11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K81) mutation to A: Abolishes activity on mandelamide.
- S180 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G178) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S180) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I183) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ K285) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ M343) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ L408) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
42% identity, 37% coverage: 15:200/506 of query aligns to 12:191/482 of 3a2qA
- active site: K69 (= K81), S147 (= S156), S148 (= S157), N166 (≠ S175), A168 (≠ T177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (= I183)
- binding 6-aminohexanoic acid: G121 (= G130), G121 (= G130), N122 (≠ A131), S147 (= S156), A168 (≠ T177), A168 (≠ T177), A169 (≠ G178), A171 (≠ S180)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 79% coverage: 51:450/506 of query aligns to 45:432/461 of 4gysB
- active site: K72 (= K81), S146 (= S156), S147 (= S157), T165 (≠ S175), T167 (= T177), A168 (≠ G178), G169 (= G179), S170 (= S180), V173 (≠ I183)
- binding malonate ion: A120 (≠ G130), G122 (= G132), S146 (= S156), T167 (= T177), A168 (≠ G178), S170 (= S180), S193 (≠ E203), G194 (≠ R204), V195 (≠ K205), R200 (≠ T210), Y297 (≠ R314), R305 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 77% coverage: 71:458/506 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K81), S170 (= S156), S171 (= S157), G189 (≠ S175), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (= I183)
- binding benzamide: F145 (≠ A131), S146 (≠ G132), G147 (≠ A133), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (≠ I313)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 44% coverage: 4:224/506 of query aligns to 1:228/564 of 6te4A
Sites not aligning to the query:
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
36% identity, 46% coverage: 7:240/506 of query aligns to 5:244/487 of 1m21A
- active site: K81 (= K81), S160 (= S156), S161 (= S157), T179 (≠ S175), T181 (= T177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ I183)
- binding : A129 (≠ G130), N130 (≠ A131), F131 (vs. gap), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ I183), I212 (= I212)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 90% coverage: 9:461/506 of query aligns to 3:411/412 of 1o9oA
- active site: K62 (= K81), A131 (≠ S156), S132 (= S157), T150 (≠ S175), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ I183)
- binding 3-amino-3-oxopropanoic acid: G130 (= G155), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ I183), P359 (≠ E402)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 90% coverage: 9:461/506 of query aligns to 3:411/412 of 1ocmA
- active site: K62 (= K81), S131 (= S156), S132 (= S157), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180)
- binding pyrophosphate 2-: R113 (= R136), S131 (= S156), Q151 (≠ D176), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ I183), P359 (≠ E402)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 94% coverage: 26:502/506 of query aligns to 37:503/605 of Q936X2
- K91 (= K81) mutation to A: Loss of activity.
- S165 (= S156) mutation to A: Loss of activity.
- S189 (= S180) mutation to A: Loss of activity.
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
32% identity, 42% coverage: 12:222/506 of query aligns to 81:287/579 of Q9TUI8
- S217 (= S156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D176) mutation D->E,N: Loss of activity.
- S241 (= S180) mutation to A: Loss of activity.
- C249 (= C188) mutation to A: Loss of activity.
Query Sequence
>HSERO_RS21870 FitnessBrowser__HerbieS:HSERO_RS21870
MQDKLVEKSAVELRQLIGSKQLSPVELLEACIARIEDINPHINAVTATCFERARGEARAA
EQAVIDGKPLGLLHGLPIGIKDLEETEGLLTTYGSPLYRGNIPARDNALVARLRAAGAIV
AGKTNVPEMGAGANSRNAVWGATGNPFNPLLNAGGSSGGSAAALATDLLPLCSGSDTGGS
LRIPAAKCGVVGFRPSPGLVPSERKLLGWTPISVVGPMGRDVADTVLQLRATLGLHASDP
LGYAVSDSEFASLPQVDLSQLRIGYTEDFGVCDVDNGIRQVFRDKMAAIAPYVKLCEPVD
VDMGEAHRAFDVIRAEAFVAGFDAAYRRDPASLGPNTRANYEMGAAMSLLDCAWAQSEQT
RIFRRFQQLYERYDLILSPTTPVSPFPWSELYLKEVNGVALENYYRWLALTYVVTLATNP
AISLPCGRDHRGMPFGLQVTGPFRGDARVLACAAALEQAFAGNETLRRPRPDLTKLKTVH
APLTSIVTDPPLLQGQGTEQSGGPAV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory